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Database: UniProt
Entry: H3DR59_TETNG
LinkDB: H3DR59_TETNG
Original site: H3DR59_TETNG 
ID   H3DR59_TETNG            Unreviewed;      1792 AA.
AC   H3DR59;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   SubName: Full=Kinesin family member 1B {ECO:0000313|Ensembl:ENSTNIP00000023008.1};
OS   Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS   nigroviridis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX   NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000023008.1, ECO:0000313|Proteomes:UP000007303};
RN   [1] {ECO:0000313|Proteomes:UP000007303}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15496914; DOI=10.1038/nature03025;
RA   Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA   Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA   Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA   Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA   Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA   Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA   Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA   McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA   Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA   Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA   Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT   "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT   early vertebrate proto-karyotype.";
RL   Nature 431:946-957(2004).
RN   [2] {ECO:0000313|Ensembl:ENSTNIP00000023008.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cell projection, axon
CC       {ECO:0000256|ARBA:ARBA00004489}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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DR   Ensembl; ENSTNIT00000023250.1; ENSTNIP00000023008.1; ENSTNIG00000015171.1.
DR   GeneTree; ENSGT00940000157445; -.
DR   Proteomes; UP000007303; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR   GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR   GO; GO:0048731; P:system development; IEA:UniProt.
DR   CDD; cd01365; KISc_KIF1A_KIF1B; 1.
DR   CDD; cd01233; PH_KIFIA_KIFIB; 1.
DR   Gene3D; 2.60.200.20; -; 1.
DR   Gene3D; 6.10.250.2520; -; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR000253; FHA_dom.
DR   InterPro; IPR022164; Kinesin-like.
DR   InterPro; IPR022140; Kinesin-like_KIF1-typ.
DR   InterPro; IPR032405; Kinesin_assoc.
DR   InterPro; IPR019821; Kinesin_motor_CS.
DR   InterPro; IPR001752; Kinesin_motor_dom.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR049780; PH_KIFIA_KIFIB.
DR   InterPro; IPR008984; SMAD_FHA_dom_sf.
DR   PANTHER; PTHR47117:SF2; KINESIN-LIKE PROTEIN KIF1A ISOFORM X1; 1.
DR   PANTHER; PTHR47117; STAR-RELATED LIPID TRANSFER PROTEIN 9; 1.
DR   Pfam; PF12473; DUF3694; 1.
DR   Pfam; PF00498; FHA; 1.
DR   Pfam; PF12423; KIF1B; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   Pfam; PF16183; Kinesin_assoc; 1.
DR   Pfam; PF00169; PH; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00240; FHA; 1.
DR   SMART; SM00129; KISc; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00283}; Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW   Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00283}; Reference proteome {ECO:0000313|Proteomes:UP000007303};
KW   Synapse {ECO:0000256|ARBA:ARBA00023018}.
FT   DOMAIN          5..357
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   DOMAIN          1670..1768
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          1518..1538
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1590..1631
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          637..679
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         97..104
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1792 AA;  201828 MW;  46CB0922164D70E7 CRC64;
     MSGASVKVAV RVRPFNSREM NMDAKCIIHM QGNSTTISNP KAPKEPAKNF SFDYSYWSHT
     TLEDPNFASQ NRVYNDIGKE MLEHAFEGYN VCIFAYGQTG AGKSYTMMGK QEEGQEGIIP
     MLCEDLFEKI NEENNKEELS YSVEVSYMEI YCERVRDLLN PKNKGNLRVR EHPLMGPYVE
     DLSKLAVTSY TDIADLMDAG NKARTVAATN MNETSSRSHA VFTIVFTQKK HDSETDLSTE
     KVSKISLVDL AGSERADSTG AKGTRLKEGT NDRRQACCNV CHSVFSFLCH ADNCTNKSKK
     KKKTDFIPYR DSVLTWLLRE NLGGNSRTAM VAALSPADVN YDETLSTLRY ADRAKNIKCN
     AVINEDPNNK LVRDLKDEVS RLKELLRAQG LGDILDTPLG SLTASPSYCS YEPALTIRAA
     VSIATTVASV SSSDVKHLHR YRESEKIIAE LNETWEEKLR KTEAIRMESS FFLPPQGGLR
     EDGGTLGVFS PKKTPHLVNL NEDPLMSECL LYYIKDGITR VGQADAERRQ DIVLSGAHIK
     EEHCIFRSER NANGDVVVLL VPCEASETYV NGKRVEDAIQ LRSGNRIIMG NHVFRFNHPE
     QARAEREKTP SAETPMEPVD WTFAQRELLE KQGIDMKQEM EKRLTEMEIL YKKEKEEADQ
     LLEQQRLVYE SKLQELQKQV ETISLVAETP DEEELDEEEE EEVPWTQHEF ELAQWAFRKW
     RYHQFTSLRD QLWGNAVYLK EANAISVELK KKVQFQFVLL TDTLYSPLPP ELGSPEPEKE
     RDPRPFPRTV VAVEVQDLKN GATHYWSLDK LKQRLEKMRE MYDRAGEMTS TNQEEGEGTL
     TGNDPFYDRF HWFKLVGSSP IFHGCVNEHL ADRTPSPTFS TTDSEITEMA DERQSEMSDL
     IDDEAFVDDT SSDAGTEEGS DIFSDGQDPF YDRSPWFILV GRAFVYLSNL LYSVPLVHRV
     AIVTEKGEVR GFLRVGVQAI AADEEAPDYG SGVRQSGTAK ISFDDEYFKK NDFPSTVMTR
     SGMSLEELRI VEGQGQSSEV ITPSEELNRI NDIDLKLGNV ADTKLSRDGL AGQLEVGSIF
     TFRVTVLQAS GIQPEYADIF CQFNFLHRHD EAFSTEPLKN TGKGTPLGFY HVQNISVEVT
     ESFVEYIKSK PIVFEVFGHY QQHPLHLHGQ ELISPPTQSR KYYPIPMPLS KPVPATKLNT
     ITKSNLGQCV SKYDLLVWFE ISELEPTGEY IPAIVDHSGG LPCHGTYLLH QGIQRRITVT
     LIHEKGSELH WKDVRELVVG RIRNKAEVDD SASDGVLSLN IISAKNIKSS HNSNRTFYRF
     EAVWDSSLHN SLLLNRVTPY GEKIYMTLSA YLELDHCIQP AIITKDICMV FYSRDAKISP
     PRSLRNLFVS GYSKTPDCNR VTGIYELSLC KMSDTGSPAG MQRRRRKVLD TSVAYVRGEE
     NLAGWRPRGD SLIAEHQWEL EKMEQLHEVE KTRHLLLLRE KLGDANPAPS TKSLSELLSP
     SMSSGTLSTS TSISSQISST TFESAITPSE SSGYDSTDIE SLVDREKALA TKCLRLLTHT
     FNSEYNQVVN SISDCKLSDI SALGRDPSVT SFSSATLTPS STCPSLADSR CGSIDQKTPE
     NSSRASSPSC SDYENFPMVP SLETSYLARA GKNEFLNLVP DIEEMRPGSV VSKKGFLSFM
     EPRSNSWVKH FVVVRRPYVF IYNSDKDPVE RGVLNLSTAQ VEYSEDQQAM LKTPNTFAVC
     TKHRGILLQA LNEKDMNDWL YAFNPLLAGT IRPLNFSSPI ICKEMSISVS FV
//
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